Isolation of phosvitin from the plasma of the laying hen

Heald, P. J.; McLACHLAN, P. M.

doi:10.1042/bj0870571

Cited by 78 publications

(23 citation statements)

References 11 publications

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“…1; J. L. Christmann, M. G. Grayson, and R. C. C. Huang, personal communication). This protein is-normally synthesized in the liver of the laying hen and is transported through the blood to the oviduct, where it is deposited in the developing oocyte (2). Vitellogenin is not normally synthesized by immature chickens or by roosters, but its synthesis can be induced in these animals by estrogen (3)(4)(5).…”

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confidence: 99%

Induction of vitellogenin synthesis by estrogen in avian liver: relationship between level of vitellogenin mRNA and vitellogenin synthesis.

Mullinix¹,

Wetekam²,

Deeley³

et al. 1976

Proc. Natl. Acad. Sci. U.S.A.

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We have investigated the estrogen-mediated induction of vitellogenin synthesis in rooster liver. We compared the concentrations of vitellogenin messenger RNA (mRNA) in the liver with the concentrations of vitellogenin in the sera of roosters that had received various treatments with estrogen. We found no vitellogenin mRNA in the livers of the unstimulated roosters. An initial injection of estrogen was attended by de novo synthesis of vitellogenin mRNA in the liver and accumulation of vitellogenin in the serum. When vitellogenin was no longer present in the serum or liver (the "post-estrogen-serum-negative" state), the liver was found to contain appreciable amounts of vitellogenin mRNA. This mRNA was of the same size as that found in the liver of the rooster actively synthesizing vitellogenin in response to estrogen. Whereas vitellogenin mRNA was in large polysomes in the livers of the roosters actively synthesizing vitellogenin, the vitellogenin mRNA in the liver of the post-estrogen-serum-negative rooster was not associated with polysomes. The possible relevance of these findings to the fact that the rooster responds differently to a primary stimulation with estrogen than to subsequent stimulations is discussed.

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confidence: 99%

Induction of vitellogenin synthesis by estrogen in avian liver: relationship between level of vitellogenin mRNA and vitellogenin synthesis.

Mullinix¹,

Wetekam²,

Deeley³

et al. 1976

Proc. Natl. Acad. Sci. U.S.A.

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“…Estrogenization also caused hyperlipernia (31-39), hypercalce mia (23,31,32,41,44,46,48,50,51), and appearances of serum vitellin (20,49,52) and a phosphoprotein (40, [45][46][47]51). The phosphoprotein was proved to be phosvitin (28,29) which had been found as one of the yolk proteins (53). It is now accepted that serum vitellin and phosvitin exist in serum as a lipovitell in-phosvitin-y-livetin complex (24).…”

Section: Discussionmentioning

confidence: 99%

“…These data suggest the possibility that plasma mercury of laying quail exists as a form which is hardly excreated into feces and urine buttransported into yolk. Efjcct of cstrogenization on retention of mercury: There are many studies on changes in the composition of plasma or sera of birds by the onset of laying (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30) and by estro genization (20,23,. In many of birds, the onset of laying caused changes in the majority of the constituents in plasma or sera, such as increases in total lipids (15)(16)(17) and total calcium (13,14,18,23) and appearances of serum vitellin (15,16,18,22,23) and a phosphoprotein (15)(16)(17).…”

Section: Discussionmentioning

confidence: 99%

Effect of Estrogenization on the Distribution of Radiomercury in Quail

Nishimura

Urakawa

1972

Jpn.J.Pharmacol

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It is known that mercury derivatives are transported into eggs developing in the reproduc tive organs of birds (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)). An egg consists of three components; yolk which develops in the ovary, albumen and shell which are secreted from the site of magnum and the site of uterus of the oviduct, respectively (13). It is known also that alkoxy mercury deriva tives (9, 10) and inorganic mercury (10, 12) are transported mostly into egg yolk, and alkyl mercury compounds into egg albumen (1, 3, 5, 6, 10) and shell (1). The difference in the mode of the transportation may be due to the difference in chemical form among these mercurials (9, 12).
On the other hand, the onset of laying in domestic fowls is accompanied by changes in the majority of the plasma components (13-30). Similar changes in the plasma were induced in immature pullets, nonlaying hens, cockerels, and other birds by treatment with estrogens (20,23,. Large quantities of phospholipids and phosphoprotein in the serum of the laying hen are synthesized in the liver in response to estrogens (20,49,52), and the phospholipids and the phosphoprotein are transported and accumulated into ovarian follicles (20).
Rissanen and Mietinen reported that inorganic mercury or alkoxy mercury derivatives possibly bound to the yolk proteins (9). These forms of mercurials would be transported into ovarian follicles via the circurating blood plasma in a yolk-protein bound form. There is a possibility that retention of mercury in birds may be controlled by treatment with es trogens. In this paper, the effect of estrogenization on distribution of radiomercury is compared between male and immature female quail and laying quail, and interrelationship among all the four entities, i.e., laying plsama, estrogens, plasma radiomercury, and yolk radiomercury, is discussed. METHODSQuail (Coturnix coturnix japonica) used in this experiment were of the JQ-NIBS closed strain and were supplied by the Nippon Institute for Biological Science Tachikawa. Both immature female and adult male quail of 4 and 6 weeks, respectively, were employed.Weight was approx. 90 g each while the laying quail weighed approx. 130 g. Quail which

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“…These lipoproteins closely resemble the low density (LDF) and the high density lipoprotein fractions of egg yolk. There are strong similarities with respect to the lipid [4,5] , carbohydrate [5,6] , and protein [7,8] components, and identical antigens occur in equivalent lipoproteins from the two sources. Such marked similarities of composition, together with the lack of substantial lipid-synthesising systems in the hen ovary [9], indicate that the ovary probably takes these lipoproteins directly from the blood and incorporates them relatively unchanged into the egg yolk.…”

Section: Introductionmentioning

confidence: 99%